the rate-limiting steps are different in the degradative and biosynthetic thiolases. Thiolases share a structurally conserved thiolase core domain composed of topologically similar N-terminal and C-terminal subdomains and a more variable loop domain with structural features involved in the tetramerization and substrate specificity
the enzyme is involved in acyclic terpenes utilisation and leucine/isovalerate utilisation pathways which are connected by the beta-oxidation phase, overview
the enzyme PaaJ is involved in the aerobic phenylacetate catabolic pathway. PaaJ, a beta-ketothiolase, transforms the resulting beta-keto C8 intermediate with CoA to the C6 intermediate dehydroadipyl-CoA and acetyl-CoA, besides catalyzing the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA
the enzyme PaaJ is involved in the aerobic phenylacetate catabolic pathway. PaaJ, a beta-ketothiolase, transforms the resulting beta-keto C8 intermediate with CoA to the C6 intermediate dehydroadipyl-CoA and acetyl-CoA, besides catalyzing the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA
Elovl-5 knockdown decreases elongation of 16:1,n-7. Elovl-5 over-expression increases synthesis of 18:1,n-7, however, this is dependent on stearoyl-CoA desaturase driven 16:1,n-7 availability
knockdown of Elovl-6 decreases elongation of 16:0 and 16:1,n-7, resulting in accumulation of 16:1,n-7. Elovl-6 over-expression preferentially drives synthesis of 16:0 elongation products 18:0 and 18:1,n-9 but not 18:1,n-7
in mice deficient for isoform Thb, the degree of induction of peroxisomal beta-oxidation of palmitate mediated by Wy14,643, a synthetic compound activating nuclear hormone receptor PPARalpha, is significantly reduced in mice deficient for Thb, while mitochondrial beta-oxidation is unaltered. The thiolase step alone is responsible for the reduced peroxisomal beta-oxidation of fatty acids. Peroxisome proliferation in the liver after Wy-treatment is normal in Thb -/- mice
isoform KAT2 positively regulates abscisic acid signaling in all the major abscisic acid responses, including abscisic acid-induced inhibition of seed germination and post-germination growth arrest, and abscisic acid-induced stomatal closure and stomatal opening inhibition in Arabidopsis thaliana. KAT2 is shown to be important for reactive oxygen species production in response to abscisic acid. Additionally, KAT2 may function downstream of transcription repressor WRKY40, which may link KAT2 with abscisic acid receptor ABAR/CHLH-mediated signaling
loss-of-function mutations of the ketoacyl thiolase gene kat-1 result in an increased accumulation of the lipofuscin-like fluorescent aging pigment, shortened lifespan, early behavioral decline, and other abnormalities characteristic of premature aging. Isoform kat-1 is required for the extension of lifespan and enhanced thermotolerance mediated by extra copies of the deacetylase gene sir-2.1. kat-1 acts independently of other known pathways that affect longevity
thiolases are enzymes which are involved in lipid metabolism, catalysing the biological Claisen condensation and thiolytic cleavage reactions using a cysteine thiol in the active site. The enzyme catalyzes the last step of the mitochondrial beta-oxidation pathway and is also involved in the synthesis of acetoacetyl-CoA for the generation of ketone bodies, cf. EC 2.3.1.9
FadA is the bta-subunit of heterotetrameric TFE catalyzing the last three steps of the beta-oxidation. When expressed separately, TFE-alpha is a catalytically active monomer whereas TFE-beta is inactive. When mixed together, active TFE tetramer is reconstituted
histone H2A.Z-bound chromatin is associated with the oxoglutarate dehydrogenase (OGDH) and acetyl-CoA acyltransferase 2 (ACAA2). Knockout of H2A.Z in HAP1 cells reduces chromatin association of OGDH and ACAA2 and posttranslational histone modifications
the nucleophilic cysteine attacks the beta-carbon of the 3-ketoacyl-CoA and becomes covalently modified. Another cysteine, Cys382, acts first as an acid providing a proton for the leaving acetyl-CoA and next as a base abstracting a proton from the incoming CoA. The activated CoA molecule then attacks the carbonyl C atom of the acylated cysteine and the fatty acyl-CoA is released. The cysteine acting as the nucleophile is activated by a conserved histidine residue (His352)
the nucleophilic cysteine attacks the beta-carbon of the 3-ketoacyl-CoA and becomes covalently modified. Another cysteine, Cys382, acts first as an acid providing a proton for the leaving acetyl-CoA and next as a base abstracting a proton from the incoming CoA. The activated CoA molecule then attacks the carbonyl C atom of the acylated cysteine and the fatty acyl-CoA is released. The cysteine acting as the nucleophile is activated by a conserved histidine residue (His352)